O-PHOSPHORYLETHANOLAMINE AMMONIA LYASE, A NEW PYRIDOXAL PHOSPHATE-DEPENDENT ENZYME

被引：13

作者：

FLESHOOD, HL

PITOT, HC

机构：

[1] McArdle Laboratory, University of Wisconsin Medical School, Madison

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 36卷 / 01期

关键词：

D O I：

10.1016/0006-291X(69)90656-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

O-phosphorylethanolamine ammonia lyase, a new enzyme present in vertebrate liver, has been shown to catalyze the catabolism of O-phosphorylethanolamine to equimolar quantities of ammonia, acetaldehyde, and inorganic phosphate. The enzyme occurs in the soluble fraction of the cell and has been partially purified from rabbit liver. Using 14C O-PE as substrate, the 14C acetaldehyde formed enzymatically was characterized as the 2,4-dinitrophenylhydrazone by infrared spectra and chromatography. Ethanolamine is not a substrate for the enzyme nor does the cobamide coenzyme affect its rate. The Km for O-phosphorylethanolamine was found to be 6.1 × 10-4M and for pyridoxal phosphate 2.7 × 10-7M. © 1969.

引用

页码：110 / &

共 19 条

[1]

BAGINSKI ES, 1967, CLIN CHEM, V13, P326

[2] PYRIDOXIN DEFICIENCY IN THE RAT - LIVER L-CYSTEIC ACID DECARBOXYLASE ACTIVITY AND URINARY AMINO-ACIDS [J].